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Structure and biological activity of basement membrane proteins

European Journal of Biochemistry · 1989 · Vol. 180(3) · pp. 487–502
Rupert Timpl

Abstract

Collagen type IV, laminin, heparan sulfate proteoglycans, nidogen (entactin) and BM-40 (osteonectin, SPARC) represent major structural proteins of basement membranes. They are well-characterized in their domain structures, amino acid sequences and potentials for molecular interactions. Such interactions include self-assembly processes and heterotypic binding between individual constituents, as well as binding of calcium (laminin, BM-40) and are likely to be used for basement membrane assembly. Laminin, collagen IV and nidogen also possess several cell-binding sites which interact with distinct cellular receptors. Some evidence exists that those interactions are involved in the control of cell behaviour. These observations have provided a more defined understanding of basement membrane function and the definition of new research goals in the future.

Cell Adhesion Molecules ResearchProtease and Inhibitor MechanismsS100 Proteins and AnnexinsLamininBasement membraneOsteonectinCell biologyPerlecanChemistryBiochemistryGlycoproteinType IV collagenMembrane

MeSH terms

AnimalsBasement MembraneHumansMembrane ProteinsStructure-Activity Relationship

Funding

  • Fritz Thyssen Stiftung
Citations
971
FWCI
19.72
field-weighted impact
References
209
Percentile
100%
vs. same field & year
Citations per year
References
Laminin–a glycoprotein from basement membranes.
Journal of Biological Chemistry · 1979 · 2,370 citations
Biological activities of laminin
Journal of Cellular Biochemistry · 1985 · 466 citations
Basement membrane complexes with biological activity
Biochemistry · 1986 · 1,500 citations
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